期刊
SCIENCE
卷 347, 期 6223, 页码 775-778出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1261833
关键词
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资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- Japan Science and Technology-Core Research for Evolutionary Science and Technology
- Japan New Energy and Industrial Technology Development Organization
- National Institute of Biomedical Innovation
- Grants-in-Aid for Scientific Research [24113001, 22227004, 26440024] Funding Source: KAKEN
The C-terminal region of Clostridium perfringens enterotoxin (C-CPE) can bind to specific claudins, resulting in the disintegration of tight junctions (TJs) and an increase in the paracellular permeability across epithelial cell sheets. Here we present the structure of mammalian claudin-19 in complex with C-CPE at 3.7 angstrom resolution. The structure shows that C-CPE forms extensive hydrophobic and hydrophilic interactions with the two extracellular segments of claudin-19. The claudin-19/C-CPE complex shows no density of a short extracellular helix that is critical for claudins to assemble into TJ strands. The helix displacement may thus underlie C-CPE-mediated disassembly of TJs.
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